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Protein

Protein O-glucosyltransferase 1

Gene

POGLUT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076). Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (PubMed:27807076). Notch glucosylation does not affect Notch ligand binding (PubMed:21490058). Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (By similarity).By similarity4 Publications

Catalytic activityi

UDP-alpha-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine.1 Publication

Kineticsi

  1. KM=72 µM for UDP-Glc1 Publication
  1. Vmax=7.6 pmol/min/µg enzyme1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.3 Publications
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • glucosyltransferase activity Source: MGI
  • protein xylosyltransferase activity Source: UniProtKB-EC
  • UDP-glucosyltransferase activity Source: UniProtKB
  • UDP-xylosyltransferase activity Source: UniProtKB

GO - Biological processi

  • axial mesoderm development Source: Ensembl
  • cardiovascular system development Source: Ensembl
  • gastrulation Source: UniProtKB-KW
  • glycolipid metabolic process Source: GO_Central
  • muscle tissue development Source: UniProtKB
  • paraxial mesoderm development Source: Ensembl
  • positive regulation of Notch signaling pathway Source: UniProtKB
  • protein O-linked glycosylation Source: MGI
  • protein O-linked glycosylation via serine Source: UniProtKB
  • regulation of gastrulation Source: UniProtKB
  • somitogenesis Source: Ensembl

Keywordsi

Molecular functionDevelopmental protein, Glycosyltransferase, Transferase
Biological processGastrulation

Enzyme and pathway databases

ReactomeiR-HSA-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
SIGNORiQ8NBL1.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT90. Glycosyltransferase Family 90.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein O-glucosyltransferase 1Curated (EC:2.4.1.-2 Publications)
Alternative name(s):
CAP10-like 46 kDa protein1 Publication
Short name:
hCLP461 Publication
KTEL motif-containing protein 1
Myelodysplastic syndromes relative protein
O-glucosyltransferase Rumi homolog1 Publication
Short name:
hRumi1 Publication
Protein O-xylosyltransferase POGLUT1Curated (EC:2.4.2.261 Publication)
Gene namesi
Name:POGLUT1Imported
Synonyms:C3orf9Imported, CLP461 Publication, KTELC1, MDSRP
ORF Names:MDS010, UNQ490/PRO10061 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:22954. POGLUT1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: UniProtKB
  • extracellular exosome Source: UniProtKB

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Dowling-Degos disease 4 (DDD4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Dowling-Degos disease, a genodermatosis manifesting with postpubertal reticulate hyperpigmentation that is progressive and disfiguring, and small hyperkeratotic dark brown papules that affect mainly the flexures and great skin folds. Patients usually show no abnormalities of the hair or nails. DDD4 is characterized by prominent involvement of non-flexural skin areas.
See also OMIM:615696
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_077954170G → E in DDD4. 1 Publication1
Natural variantiVAR_077955218 – 392Missing in DDD4. 1 PublicationAdd BLAST175
Natural variantiVAR_077957286C → Y in DDD4. 1 Publication1
Limb-girdle muscular dystrophy 2Z (LGMD2Z)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of autosomal recessive limb-girdle muscular dystrophy, a degenerative myopathy characterized by slowly progressive wasting and weakness of the proximal muscles of arms and legs around the pelvic or shoulder girdles, elevated creatine kinase levels and dystrophic features on muscle biopsy. LGMD2Z is characterized by young-adult onset.
See also OMIM:617232
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_077956233D → E in LGMD2Z; reduced glucosyltransferase and xylosyltransferase activities; impaired Notch signaling. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi169G → E: Loss of O-glucosyltransferase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

DisGeNETi56983.
MalaCardsiPOGLUT1.
MIMi615696. phenotype.
617232. phenotype.
OpenTargetsiENSG00000163389.
Orphaneti79145. Dowling-Degos disease.
PharmGKBiPA162393771.

Polymorphism and mutation databases

BioMutaiPOGLUT1.
DMDMi74730148.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000024668524 – 392Protein O-glucosyltransferase 1Add BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi373N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ8NBL1.
MaxQBiQ8NBL1.
PaxDbiQ8NBL1.
PeptideAtlasiQ8NBL1.
PRIDEiQ8NBL1.

PTM databases

iPTMnetiQ8NBL1.
PhosphoSitePlusiQ8NBL1.

Expressioni

Tissue specificityi

Expressed in most adult tissues at different intensities. Abundantly expressed in liver. Expressed also in brain, heart, skeletal muscle, spleen, kidney, placenta, lung and peripheral blood leukocyte. Not detectable in colon, thymus and small intestine. Expressed in the epidermis, especially in the upper parts, stratum spinosum and stratum granulosum (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000163389.
CleanExiHS_KTELC1.
ExpressionAtlasiQ8NBL1. baseline and differential.
GenevisibleiQ8NBL1. HS.

Organism-specific databases

HPAiHPA037855.

Interactioni

Protein-protein interaction databases

BioGridi121300. 27 interactors.
STRINGi9606.ENSP00000295588.

Structurei

3D structure databases

ProteinModelPortaliQ8NBL1.
SMRiQ8NBL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi389 – 392Prevents secretion from ERPROSITE-ProRule annotation4

Sequence similaritiesi

Belongs to the glycosyltransferase 90 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2458. Eukaryota.
ENOG410XT5U. LUCA.
GeneTreeiENSGT00530000063132.
HOVERGENiHBG069044.
InParanoidiQ8NBL1.
KOiK13667.
OMAiIPLVDHC.
OrthoDBiEOG091G0BPU.
PhylomeDBiQ8NBL1.
TreeFamiTF323280.

Family and domain databases

InterProiView protein in InterPro
IPR006598. LipoPS_modifying.
PfamiView protein in Pfam
PF05686. Glyco_transf_90. 1 hit.
SMARTiView protein in SMART
SM00672. CAP10. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8NBL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWWASSPLR LWLLLFLLPS AQGRQKESGS KWKVFIDQIN RSLENYEPCS
60 70 80 90 100
SQNCSCYHGV IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ ITKNRLYREN
110 120 130 140 150
DCMFPSRCSG VEHFILEVIG RLPDMEMVIN VRDYPQVPKW MEPAIPVFSF
160 170 180 190 200
SKTSEYHDIM YPAWTFWEGG PAVWPIYPTG LGRWDLFRED LVRSAAQWPW
210 220 230 240 250
KKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ AWKSMKDTLG
260 270 280 290 300
KPAAKDVHLV DHCKYKYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWLEF
310 320 330 340 350
FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDVAQEIAE RGSQFIRNHL
360 370 380 390
QMDDITCYWE NLLSEYSKFL SYNVTRRKGY DQIIPKMLKT EL
Length:392
Mass (Da):46,189
Last modified:October 1, 2002 - v1
Checksum:i25B0370757A6B224
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti287G → D in BAD96657 (Ref. 5) Curated1
Sequence conflicti371S → P in BAD96657 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02704175K → R1 PublicationCorresponds to variant dbSNP:rs11556605Ensembl.1
Natural variantiVAR_077954170G → E in DDD4. 1 Publication1
Natural variantiVAR_077955218 – 392Missing in DDD4. 1 PublicationAdd BLAST175
Natural variantiVAR_027042229P → T1 PublicationCorresponds to variant dbSNP:rs17852785Ensembl.1
Natural variantiVAR_077956233D → E in LGMD2Z; reduced glucosyltransferase and xylosyltransferase activities; impaired Notch signaling. 1 Publication1
Natural variantiVAR_077957286C → Y in DDD4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY298903 mRNA. Translation: AAP56253.1.
AY358581 mRNA. Translation: AAQ88944.1.
AK075444 mRNA. Translation: BAC11625.1.
AK222937 mRNA. Translation: BAD96657.1.
AK315367 mRNA. Translation: BAG37760.1.
AC074271 Genomic DNA. No translation available.
AC073352 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79570.1.
BC030614 mRNA. Translation: AAH30614.1.
BC048810 mRNA. Translation: AAH48810.1.
CCDSiCCDS2988.1.
RefSeqiNP_689518.1. NM_152305.2.
UniGeneiHs.231750.

Genome annotation databases

EnsembliENST00000295588; ENSP00000295588; ENSG00000163389.
GeneIDi56983.
KEGGihsa:56983.
UCSCiuc003ecm.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPGLT1_HUMAN
AccessioniPrimary (citable) accession number: Q8NBL1
Secondary accession number(s): B2RD13, Q53GJ4, Q8N2T1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2002
Last modified: June 7, 2017
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families